UV-curable methacrylated/fumaric acid modified epoxy as a potential support for enzyme immobilization

Kahraman, Memet Vezi̇r; Bayramoğlu, Gülay; Kayaman‐Apohan, Nilhan; Güngör, Atilla

doi:10.1016/j.reactfunctpolym.2006.09.005

Cited by 31 publications

(21 citation statements)

References 24 publications

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“…Even higher temperature optimum, from 30 to 50°C was observed for GAg-RSDA, AgRSDA-CROSS and Ag-RSDA-RET. This coincided with the report by Kahraman et al (2007); immobilization of aamylase through covalent attachment on functionalized glass beads shifted the temperature optima from 30°C for the free enzyme to 50°C for the immobilized amylase. Our report indicates greater rigidity of the immobilized enzyme resulting to a bound molecule that is more resistance to unfolding at higher temperatures.…”

Section: Immobilization On Temperature Activity and Stabilitysupporting

confidence: 92%

Stabilization of a raw starch digesting amylase from Aspergillus carbonarius via immobilization on activated and non-activated agarose gel

Nwagu

Okolo

Aoyagi

2011

World J Microbiol Biotechnol

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Applications of raw starch digesting amylases (RSDAs) are limited due to instability, product inhibition of enzyme and contamination. RSDA from Aspergillus carbonarius was stabilized through immobilization on agarose gel by adsorption, spontaneous crosslinking and conjugation using glycidol, glutaraldehyde or polyglutaraldehyde. Effects of immobilization on kinetics, catalytic, storage and operational stability of immobilized enzyme were evaluated. Polyglutaraldehyde activated agarose RSDA (PGAg-RSDA) gave the highest immobilization yield (100%) with expressed activity of 86.7% while that of glycidol activated RSDA (GlyAg-RSDA) was 80.4%. A shift in pH from optimum of 5 for the soluble enzyme to 6 for RSDA adsorbed on agarose followed by crosslinking with glutaraldehyde (AgRSDA-CROSS) and simultaneous adsorption and crosslinking (AgRSDA-RET), and pH 7 for PGAg-RSDA was seen. PGAg-RSDA and AgRSDA-CROSS were most pH stable and retained over 82% of their activities between pH 3.5 and 9 compared to 59% for the soluble enzyme. Thermoinactivation studies showed that immobilized RSDAs with the exception of GAg-RSDA retained over 90% of their activities at 60°C for 120 min while soluble enzyme retained only 76% activity under the same condition. AgRSDA-CROSS, PGAg-RSDA, Gly-RSDA and GAg-RSDA retained approximately 100% of their activities after 30 days storage at 4°C. GlyAg-RSDA retained 99.6%, PGAg-RSDA 94%, AgRSDA-CROSS 90%, GAg-RSDA 86.5% and Ag-RSDA-RET 80% activity after 10 batch reactions. Immobilization stabilized RSDA and permits processing at higher temperatures to reduce contamination.

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Section: Immobilization On Temperature Activity and Stabilitysupporting

confidence: 92%

Stabilization of a raw starch digesting amylase from Aspergillus carbonarius via immobilization on activated and non-activated agarose gel

Nwagu

Okolo

Aoyagi

2011

World J Microbiol Biotechnol

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“…Polymerization reaction was carried out at 65 C for 18 h. The grafted p(VBC/EGDMA-g-GMA) beads were filtered and transferred into a solution containing EDTA solution about 10% (w/v) and it was stirred continuously to remove copper ions for 24 h. The p(VBC/EGDMA-g-GMA) beads were filtered and washed sequentially with water (1.0 L) and ethanol (500 mL). The p(VBC/EGDMA-g-GMA) beads were dried in vacuum oven at 25 C.…”

Section: Synthesis Of Poly(vinylbenzylchloride/ Ethyleneglycol Dimetamentioning

confidence: 99%

“…The modified p(VBC/EGDMA-g-GMA)-HDZ affinity beads were dried overnight under vacuum at 25 C for 24 h.…”

Section: Modification Of P(vbc/egdma-g-gma) Beads With Hydrazinementioning

confidence: 99%

“…Enzyme desorption were performed in a NaOH solution (1.0M). The enzyme adsorbed beads were placed in the cleaning medium while stirring at 100 rpm at 25 C for 2 h. The beads were removed from cleaning medium washed several times with acetate buffer (50 mM, pH 5.5) and were then reused in subsequence enzyme immobilization.…”

Section: Reusability and Storage Stability Of Enzymesmentioning

confidence: 99%

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Poly(vinylbenzylchloride) beads grafted with polymer brushes carrying hydrazine ligand for reversible enzyme immobilization

Yavuz¹,

Bayramoğlu²,

Şenkal³

et al. 2009

J of Applied Polymer Sci

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Poly(glycidylmethacrylate), p(GMA), brush grafted poly(vinylbenzyl chloride/ethyleneglycol dimethacrylate), p(VBC/EGDMA), beads were prepared by suspension polymerization and the beads were grafted with poly(glycidyl methacrylate), p(GMA), via surface-initiated atom transfer radical polymerization aiming to construct a material surface with fibrous polymer. The epoxy groups of the fibrous polymer were reacted with hydrazine (HDZ) to create affinity binding site on the support for adsorption of protein. The influence of pH, and initial invertase concentration on the immobilization capacity of the p(VBC/EGDMA-g-GMA)-HDZ beads has been investigated. Maximum invertase immobilization onto hydrazine functionalized beads was found to be 86.7 mg/g at pH 4.0. The experimental equilibrium data obtained invertase adsorption onto p(VBC/EGDMA-g-GMA)-HDZ affinity beads fitted well to the Langmuir isotherm model. It was shown that the relative activity of immobilized invertase was higher than that of the free enzyme over broader pH and temperature ranges. The K m and V max values of the immobilized invertase were larger than those of the free enzyme. After inactivation of enzyme, p(VBC/EGDMA-g-GMA)-HDZ beads can be easily regenerated and reloaded with the enzyme for repeated use.

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“…UV curing is a simple and convenient method with low energy consumption and no solvent emission. Due to the short curing times (30 seconds to 2 minutes) it cause less damage to the catalytic activity of enzyme during immobilization process 26 . For this purpose chitosan was modified with 2-isocayanatoethyl methacrylate and by this way a polymer containing urethane linkages and carbon-carbon double bonds was obtained.…”

Section: Introductionmentioning

confidence: 99%

Methacrylated Chitosan Based UV Curable Support for Enzyme Immobilization

Bayramoğlu

2017

Mat. Res.

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UV curing is simple, fast and effective procedure for enzyme immobilization with minimized enzymatic activity. UV-curable methacrylated chitosan is here proposed as a support material for immobilization of lipase. The morphology of the polymeric support was characterized by scanning electron microscopy (SEM). Both covalently (CIL) and physically (PIL) immobilized enzyme is analyzed in terms of enzymatic activity as a function of reusability, pH, storage, as well as stability under various experimental conditions. The recovery of activity of lipases immobilized onto a photocrosslinked polymer network was 82.0% and 70.0% for CIL and PIL, respectively. The optimum pH value for the free lipase was at pH 6.0. The optimum pH of the both CIL and PIL was shifted to pH 7.0. Immobilization increased the thermostability of the lipase from 50 ºC to 62 ºC. The free enzyme lost all its activity within 15 days. Repeated batch experiments show that about 61% of the enzyme activity of CIL and 41% of PIL was retained after 8 cycles.

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UV-curable methacrylated/fumaric acid modified epoxy as a potential support for enzyme immobilization

Cited by 31 publications

References 24 publications

Stabilization of a raw starch digesting amylase from Aspergillus carbonarius via immobilization on activated and non-activated agarose gel

Stabilization of a raw starch digesting amylase from Aspergillus carbonarius via immobilization on activated and non-activated agarose gel

Poly(vinylbenzylchloride) beads grafted with polymer brushes carrying hydrazine ligand for reversible enzyme immobilization

Methacrylated Chitosan Based UV Curable Support for Enzyme Immobilization

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